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PubMed1992

Thyroid peroxidase antibodies in children with autoimmune thyroiditis.

AIMS: To compare the prevalence of thyroid peroxidase antibodies in 25 children with autoimmune thyroid disorders and in 41 children and young adults with type 1 diabetes, and to test the prevalence of thyrotropin receptor antibodies. METHODS: Two commercially available radioimmunoassays for antibodies to thyroid peroxidase, a commercially available agglutination test of particles coated with thyroid microsomal antigens, and a radioimmunoassay for thyrotropin receptor antibodies were used. Patients and controls were studied. RESULTS: One of the radioimmunoassays detected thyroid peroxidase antibodies not only in all children with autoimmune thyroid disorders and children and young adults with type 1 diabetes and thyroid microsomal antibodies, but also in 20% of healthy control children without microsomal antibodies. With this thyroid peroxidase assay and with microsomal agglutination, 94% of the children with autoimmune thyroiditis, 71% of those with Graves' disease, and over 90% of those with type 1 diabetes and thyroid dysfunction tested positive. In the other radioimmunoassay for thyroid peroxidase antibodies thyroid peroxidase antibody titres in half or more of the children with microsomal antibodies failed to reach the level of positivity given by the producers. Eighty five percent of children with Graves' disease and 71% of those with autoimmune thyroiditis had thyrotropin receptor antibodies but so did 35% of children studied for other endocrinological disorders such as delayed growth or puberty. CONCLUSIONS: Testing patients with well characterised disorders of thyroid function and with other endocrine disorders is important in evaluating the efficacy of new diagnostic tests for thyroid autoantibodies.

Adolescent↗
PubMed1994

cDNA sequence and tissue-specific expression of an anionic flax peroxidase.

A flax (Linum usitatissimum L.) lambda gt10 cDNA library was screened with a probe coding for the amino terminus of a flax peroxidase. The probe was generated by PCR amplification of the library with one of the lambda gt10 sequencing primers and a mixed oligonucleotide derived from a well-conserved amino acid region (distal heme ligand) found in all plant peroxidases. A positive clone (FLXPER2) was isolated and characterized. The cDNA contains 1153 nucleotides, excluding the poly(A) tail, and encodes a mature protein of 297 amino acids with a molecular mass of 31.9 kDa. The mature protein's amino acid sequence contains three highly conserved regions, two of which contain histidine ligands for the heme group. The deduced amino acid sequence has nine cysteine residues. Eight are identically located to those of horseradish C peroxidase, which participate in four disulfide bridges; these cysteines are highly conserved in all plant peroxidases. One potential N-glycosylation site (Asn-X-Thr/Ser) is present. The predicted pI value of 4.5 identifies FLXPER2 as an anionic peroxidase. Northern blot analysis shows that its mRNA expression is unique to stem tissue. Amino acid sequence comparisons show high similarity between FLXPER2 and peanut, rice, and tobacco peroxidases.

Amino Acid Sequence↗
PubMed1979

Ascorbate and peroxidase changes during pregnancy in albino rat and Swiss mouse.

From the 1st to 6th days of pregnancy in the rat, while the blastocyst is still in the fallopian tube, there is high peroxidase activity in the corpus luteum, the blastocyst, and there is high peroxidase activity in the endometrium. On day 8 of pregnancy, peroxidase activity in the corpus luteum begins to fall rapidly, and there is a sharp rise in the peroxidase activity of the uterine endometrium. In all these tissues an inverse relationship exists between peroxidase and ascorbate content. We suggest the involvement of the peroxidase-ascorbate system in the mechanism of the extended function of the corpus luteum during pregnancy and a role for free radicals in the process of implantation of the blastocyst in the uterus.

Animals↗
PubMedDate not supplied

Age- and gender-related differences in human lacrimal fluid peroxidase activity.

There is evidence to suggest that estrogen influences lacrimal fluid peroxidase activity in women. In this study we investigated changes in peroxidase activity related to ageing and gender. These changes might help to explain the common problem of dry-eye syndrome in menopausal women. Unstimulated tears were collected from 70 healthy subjects of both sexes (age range 24-90 years). Tear samples were collected from 9 to 10 a.m., when peroxidase activity remained stable. In women, lacrimal fluid peroxidase activity decreased significantly during the menopause (p < 0.05 by one-way ANOVA), and thereafter remained unchanged. Conversely, in men, lacrimal fluid peroxidase activity decreased later, declining significantly only towards the age of 80 (p < 0.05). Lacrimal fluid peroxidase activity differs in men and women: the gender-related difference accentuates during ageing, probably owing to changing estrogen levels.

Adult↗
PubMed1987

Endogenous peroxidase activity in human cutaneous and adenoidal mast cells.

We have studied peroxidase activity in human cutaneous and adenoidal mast cells using different methods, in order to determine the optimal technical conditions for its demonstration. In 1.25% glutaraldehyde-fixed cells, no peroxidase activity was seen. On the contrary, in tannic acid-aldehyde-fixed cells or in unfixed cells peroxidase activity was revealed independently of the DAB concentration or the incubation time in DAB medium. The reaction product was localized in perinuclear cisternae and endoplasmic reticulum. Granules were always unreactive with all techniques employed. Golgi apparatus was generally negative and only occasional cells exhibited one or two positive peripheral cisternae. This activity appears sensitive to fixation by glutaraldehyde and is inhibited by 3-amino-1,2,4-triazole (AMT) and by lack of H2O2 or DAB in the incubation medium, but not by potassium cyanide, sodium azide, or sodium pyruvate, at the concentrations used. The peroxidase activity described in this report is an endogenous peroxidase and is not related to uptake of exogenous peroxidase by mast cells. It can therefore be considered as an ultracytochemical marker of human mast cells.

Adenoids↗
PubMed1981

Calcium requirement for the secretion of peroxidases by plant cell suspensions.

Spinach (Spinacia oleracea, L.) cells in liquid culture release peroxidases. This release is reduced by EGTA and promoted by calcium ions. In a medium deprived of calcium the rate of peroxidase release is low, but immediately after addition of I mM calcium there is a sudden increase of the extracellular peroxidase activity. Extracellular calcium apparently penetrates into the cultured cells rather freely and, as a consequence, the rate of peroxidase secretion by these cells is directly correlated with the concentration of calcium in the medium. Magnesium, at twice the concentration used for calcium, has no effect on the release of peroxidases. Cells treated with Na azide, Na hydrogenarsenate of fluphenazine secrete less peroxidase upon addition of calcium.

Calcium↗
PubMed1986

Stylar peroxidase and incompatibility reactions in Petunia hybrida.

Self-, cross- and non-pollinated styles of Petunia hybrida were treated with 3-3'-diaminobenzidine for the ultrastructural localization of peroxidase activity. Wall peroxidases were absent in cross-pollinated styles, but they were detectable as an osmiophilic deposit on the cell walls of the outer portion of the transmitting tissue in self- and non-pollinated styles. The cell layer showing peroxidase activity was thicker in the self-pollinated styles than in the non-pollinated ones. In accordance with current hypotheses on the mechanism involved in pollen incompatibility process, it is suggested: that wall peroxidases present in the cells of the outer portion of the transmitting tissue are involved in the gametophytic self-incompatibility of Petunia; that self-pollination causes an increase in the number of cells involved in the rejection process; that non-pollinated styles, which are characterized by the presence of cell wall peroxidases in the outer portion of the transmitting tissue, are 'prepared' to a certain extent for the rejection of incompatible pollen tubes. The removal of peroxidase activity thus seems to be an important step in the compatible pollination process.

Cell Wall↗
PubMed2006

Effect of copper and manganese ions on activities of laccase and peroxidases in three Pleurotus species grown on agricultural wastes.

Copper (Cu2+) and manganese (Mn2+) ions influenced laccase (Lac) and peroxidase production in Pleurotus eryngii, Pleurotus ostreatus, and Pleurotus pulmonarius. In P. eryngii, the optimum Cu2+ concentration for Lac production was 1 mM and for peroxidases 10 mM, and Mn2+ concentration of 5 mM led to peaks of Lac and peroxidase activity. In P. ostreatus HAI 493, the highest level of Lac activity was at Cu2+ concentrations of 1 and 10 mM and Mn2+ concentration of 1 mM, respectively. The absence of Cu2+ and Mn2+ caused the highest levels of peroxidase production. In P. ostreatus HAI 494, the highest level of Lac activity was at a Cu2+ concentration of 5 mM and at Mn2+ concentration of 1 mM, respectively. High levels of peroxidase activity were found in the medium without and with 1 mM Cu2+, and at 1 and 5 mM Mn2+, respectively. In P. pulmonarius, the highest Lac activity was found in the presence of 5 mM Cu2+ and 5 mM Mn2+, respectively. The absence of Cu2+ and Mn2+ as well as their presence at a concentration of 1 mM led to the peaks of peroxidase activities.

Catalysis↗
PubMed1994

Plasma glutathione peroxidase activity as an index of renal function.

The kidney is a major source of the plasma enzyme glutathione peroxidase. We measured plasma glutathione peroxidase activity in 130 patients affected with different renal diseases at various stages, and compared it with the following indices of kidney function: serum creatinine, creatinine clearance, and urinary excretion of alpha 1-microglobulin, beta 2-microglobulin, albumin and N-acetyl-beta-D-glucosaminidase. Plasma glutathione peroxidase activity appeared significantly reduced in most of the renal diseases considered, and showed a significant correlation with most of the renal function indices. Linear discriminant analysis showed that the set of indices composed of plasma glutathione peroxidase activity, serum creatinine and creatinine clearance allowed the best classification of renal diseases. During treatment with the nephrotoxic aminoglycoside, tobramycin, plasma glutathione peroxidase activity showed an early and progressive decrease. We suggest the measurement of plasma glutathione peroxidase activity as an adjunctive index for the assessment of kidney alterations.

Acetylglucosaminidase↗
PubMed1991

Enzymatic deglycosylation of porcine thyroid peroxidase: effects on catalytic activity and immunoreactivity.

Thyroid peroxidase is a heme-containing, membrane-bound, glycoprotein enzyme that catalyzes iodination and coupling in the thyroid gland. It is also the antigen for microsomal autoantibodies that are commonly found in the serum of patients with autoimmune thyroid disease. We examined the effect of deglycosylation on the catalytic functions and the immunoreactivity of this enzyme. A highly purified, solubilized, large tryptic fragment of porcine thyroid peroxidase, retaining all of the N-linked glycosylation sites of the native enzyme and displaying full catalytic activity was used. It was deglycosylated by treatment with N-glycanase under nondenaturing conditions. The loss in relative molecular mass after treatment, determined by gel electrophoresis, was about 75% of the estimated molecular weight of the glycan portion of porcine thyroid peroxidase. Lectin blots performed with horseradish peroxidase-conjugated concanavalin A showed a similar loss in relative molecular mass but some residual carbohydrate. The intensity of the carbohydrate stain was consistent with the loss of about 75% of the glycans. Despite this loss, three different assays for catalytic activity of porcine thyroid peroxidase were not significantly decreased. Immunoreactivity measured by immunoblotting and by enzyme-linked immunosorbent assay was also unimpaired. These findings suggest that N-glycanase-sensitive glycans in porcine thyroid peroxidase do not act as antigenic determinants and play a minor role, if any, in catalytic activity and, presumably therefore, in the maintenance of protein conformation.

Animals↗
PubMed1994

Thyroid peroxidase immunodetection as a tool to assist diagnosis of thyroid nodules on fine-needle aspiration biopsy.

In a previous work we have reported the presence in 96.9% of malignant and 4.2% of benign thyroid tumors of an immunological abnormality of the enzyme thyroid peroxidase, impeding the fixation of the anti-thyroid peroxidase monoclonal antibody termed "MoAb47". The present study has been designed to establish the ability of thyroid peroxidase immunodetection to assist the diagnosis of malignancy in fine-needle aspiration of thyroid nodules. The fixation of anti-thyroid peroxidase monoclonal antibody was investigated by immunohistochemistry on fine-needle aspirates of 150 surgically removed thyroid nodules (20 papillary carcinomas, five follicular carcinomas, 90 colloid adenomas, nine fetal adenoma, 13 atypical adenomas, five oncocytic adenomas, six Hashimoto's thyroiditis and two Graves' disease). The percentage of positive cells has been compared to the final histological diagnosis. In samples from 113/125 benign nodules 80-100% cells presented a positive immunoreaction, whereas all samples from malignant tumors yielded less than 80% positive cells. Benign nodules exhibiting less than 80% positive cells corresponded to three degenerative colloid nodules, five atypical follicular adenomas, two oncocytomas and two thyroiditis. According to results obtained in this series, with the value of 80% as the limit for discrimination between benign and high-risk nodules, the sensitivity of thyroid peroxidase staining for diagnosis of malignancy would be 100%, its specificity 90% and its overall accuracy 92%. Thyroid peroxidase staining with monoclonal antibody MoAb47 on fine-needle aspirates is a useful adjunct to conventional cytology for the investigation of patients with thyroid nodules.

Biopsy, Needle↗
PubMed2005

Changes in the activity of amylase, peroxidase and catalase in beech (Fagus orientalis Lipsky) during dormancy and growth.

Activities of peroxidase, amylase and catalase were analyzed on beech (Fagus orientalis Lipsky) during one year to determine relationship between these enzymes with the period of dormancy and growing season. Results showed that amylase activity was high but catalase and peroxidase activities were low during the growing season. Peroxidase and catalase activities increased from July to November whereas amylase activity started to decrease at the same time, which means that the plants were prepared themselves to be dormant and the hardening was happened. The peroxidase maximum activity was in November, which is an important sign of dormancy and completing hardening in plant. The dormancy released from February along with decrease of catalase activity. At the beginning of growing season, correlation between amylase and catalase was increased. Amylase activity also increased gradually. No significant correlation between amylase-catalase and amylase-peroxidase activities was found at the period of dormancy. In our study, we found that the seasonal activity of enzymes such as peroxidase, catalase, and amylase, also correlation between these enzymes could be an important factor for the detection the period of dormancy and growing season.

Amylases↗
PubMed2000

Effects of estrogens and androgens on erythrocyte antioxidant superoxide dismutase, catalase and glutathione peroxidase activities during the menstrual cycle.

The effects of physiological changes in estrogens and androgens on the erythrocyte antioxidant superoxide dismutase, catalase and glutathione peroxidase enzyme activities during the menstrual cycle were investigated in healthy eumenorrheic women. Blood samples were taken on alternate days from twelve normally cyclic women (age range: 20 to 27 years; mean age: 24.1 years) from the first day of one menstrual cycle until the first day of the subsequent one. Plasma was analyzed for FSH, LH, estradiol, progesterone, testosterone, free testosterone and androstenedione concentrations. Erythrocyte superoxide dismutase, catalase and glutathione peroxidase activities were evaluated on the same days and cycle length was standardized on the basis of the preovulatory estradiol peak. Significant cyclic phase-related changes were observed in glutathione peroxidase (P<0.05), with higher glutathione peroxidase activity levels from the late follicular to the early luteal phase compared with those found in the early follicular phase (P<0.001 and P<0.002 respectively). A significant positive correlation was observed between mean estradiol and glutathione peroxidase cycle-related variations (r=0.80, P<0.001), whereas no significant cycle phase-dependent changes were seen in superoxide dismutase and catalase. No effect of progesterone and androgens on the erythrocyte antioxidant enzyme system was documented. The findings indicate that physiological ovarian estradiol production during the menstrual cycle may have an important role in regulating erythrocyte glutathione peroxidase activity.

Adult↗
PubMed2006

Purification and thermal characterization of a novel peroxidase from a local chick pea cultivar.

A novel peroxidase isolated from a local chick pea (Cicer arietinum L.) cultivar (Balksar 2000) was purified by means of ammonium sulfate precipitation, DEAE-cellulose chromatography and two runs on gel filtration. The purified enzyme has a specific activity of 2045 U/mg with 17 % activity recovery. The molecular mass of the enzyme was estimated to be 39 kDa by SDS-polyacrylamide gel electrophoresis. Optimum pH and temperature of the enzyme were 5.5 and 45 degrees C respectively. The thermal denaturation of local chick pea peroxidase was studied in aqueous solution at temperatures ranging from 45 degrees C to 65 degrees C. The temperature of 50% inactivation of the enzyme was found to be 68 degrees C. The enthalpy (DeltaH*) and free energy (DeltaG*) of thermal denaturation of chick pea peroxidase were 101.4 and 103.4 k J/mol respectively at 65 degrees C. Metals like Zn2+, Mn2+, Hg2+, Co2+ and Al3+ slightly inhibited the peroxidase activity while Ca2+, Mg2+ and Ba2+ have no effect on enzyme activity. The high specific activity and thermal stability make chick pea peroxidase an alternative to horseradish peroxidase (HRP) in various applications.

Ammonium Sulfate↗
PubMed1987

Factor analysis of the activities of superoxide dismutase, catalase and glutathione peroxidase in normal tissues and neoplastic cell lines.

Exploratory factor analysis of reported specific activities of the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase in normal human tissues, normal mouse tissues, vertebrate red blood cells and neoplastic human cell lines shows that the activities of copper-zinc superoxide dismutase, catalase and glutathione peroxidase in normal tissues are influenced by a single factor. Catalase activity has the highest loading and correlation with this factor, suggesting a catalase- or hydrogen peroxide-related influence. The activity of manganese superoxide dismutase is influenced by a separate factor. The activities of copper-zinc and manganese superoxide dismutases in normal tissues therefore appear to be dichotomously regulated. The activities of superoxide dismutase and glutathione peroxidase in vertebrate red blood cells are influenced by a single factor. The activity of catalase is influenced by a separate factor. The roles of glutathione peroxidase and catalase in hydrogen peroxide catabolism in red blood cells in fact differ. In neoplastic human cell lines, two bipolar factor factors appear to influence the activities of catalase and manganese superoxide dismutase, and glutathione peroxidase and copper-zinc superoxide dismutase, respectively. The factors are, however, mainly catalase and glutathione peroxidase activity factors as the loadings and correlations of manganese superoxide dismutase on the one hand and copper-zinc superoxide dismutase on the other, with the respective factors, are relatively small. Potentially low superoxide production and intrinsically low peroxidizability of tumour cell membranes underlie the peculiar variation of antioxidant enzyme activities in tumour cells. Factor analysis is proposed as a heuristic data reduction and hypothesis-creating technique for the variation of antioxidant and other functionally-linked enzyme activities in normal and pathological cells and tissues.

Analysis of Variance↗
PubMed1988

A simultaneous visualization of the antioxidant enzymes glutathione peroxidase and catalase on polyacrylamide gels.

A simple and sensitive method for the simultaneous visualization of glutathione peroxidase and catalase on polyacrylamide gels is described. The procedure included: (1) running samples on a 7.5% polyacrylamide gel, (2) soaking the gel in a certain concentration of reduced glutathione (0.25-2.0 mM), (3) soaking the gel in GSH plus H2O2 or cumene hydroperoxide, (4) finally staining with a 1% ferric chloride 1% potassium ferricyanide solution. The best concentration of glutathione for simultaneous visualization of glutathione peroxidase in mouse liver homogenates and also it is specific for glutathione peroxidase since other peroxidases such as lactoperoxidase, horseradish peroxidase and glutathione S-transferase cannot be visualized. Using this method, it was found that unlike catalase, glutathione peroxidase is heat resistant (68 degrees C, 1 min), but sensitive to 10 mM sodium iodoacetate.

Animals↗
PubMed1984

Selenium content and glutathione peroxidase activity in tissues of the dairy cow after short-term feeding.

The effect of selenium and vitamin E on concentrations of selenium and selenium-dependent glutathione peroxidase in tissues of dairy cows was studied. Selenium (5 mg/day) and vitamin E (2 g/day) were supplemented for 10 days in a 2 X 2 factorial arrangement. Selenium supplementation increased content of selenium in whole blood, plasma, ovary, and liver and increased activity of selenium-dependent glutathione peroxidase in liver. Activity of selenium-dependent glutathione peroxidase in follicular fluid was closely correlated with selenium-dependent glutathione peroxidase in plasma. Significant activity of selenium-dependent glutathione peroxidase was detected in luteal tissue of the ovary. Relationships were linear between content of selenium and selenium-dependent glutathione peroxidase in ovary, uterus, and adrenal tissues.

Administration, Oral↗
PubMed2000

Effect of polysaccharide krestin on glutathione peroxidase gene expression in mouse peritoneal macrophages.

Polysaccharide krestin (PSK) is a protein-bound polysaccharide extracted from the sporophore Coriolus versicolor. Previously, we found that PSK could reduce the oxidative injury that oxidised low-density lipoprotein (Ox-LDL) produced in monocytes/macrophages, and therefore have some pro-phylactic or therapeutic effect on atherosclerosis. Glutathione peroxidases, including selenium-dependent glutathione peroxidase (SeGPx) and non-selenium-dependent glutathione peroxidase (non-SeGPx, also called glutathione S-transferase [GST]), play an important role in the defence against oxidative injury. In order to find out if the effects of PSK were associated with antioxidant enzymes, we investigated its effect on glutathione peroxidase activity and messenger RNA (mRNA) expression in mouse peritoneal macrophages. Results showed that PSK enhanced SeGPx and non-SeGPx activity, and increased SeGPx and GST-P (pi class GST) mRNA in mouse peritoneal macrophages. In addition, the induction by PSK of the two glutathione peroxidases could be blocked by cycloheximide (30 micrograms/mL), but 5 micrograms/mL actinomycin D and 50 micrograms/mL acetovanilone (a superoxide inhibitor) had no effect. We conclude that PSK improved glutathione peroxidase activity through transcriptional induction of mRNA expression.

Animals↗